Publications by authors named "Ezry Santiago-McRae"

Many membrane proteins are sensitive to their local lipid environment. As structural methods for membrane proteins have improved, there is growing evidence of direct, specific binding of lipids to protein surfaces. Unfortunately the workhorse of understanding protein-small molecule interactions, the binding affinity for a given site, is experimentally inaccessible for these systems.

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Motivation: Clusters of hydrophobic residues are known to promote structured protein stability and drive protein aggregation. Recent work has shown that identifying contiguous hydrophobic residue clusters (termed "blobs") has proven useful in both intrinsically disordered protein (IDP) simulation and human genome studies. However, a graphical interface was unavailable.

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Article Synopsis
  • - The study focuses on how pentameric ligand-gated ion channels (pLGICs), which help in synaptic transmission, are influenced by their surrounding lipid environment, especially phospholipids.
  • - Researchers highlight the positive modulation of the ELIC channel by the anionic phospholipid, phosphatidylglycerol, discovering that it binds uniquely when the channel is in an open state.
  • - Through structural analysis and calculations, the study suggests that phosphatidylglycerol stabilizes the open state of the ELIC channel, providing insight into the molecular mechanisms of lipid modulation in pLGICs.
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An urgent need exists for a rapid, cost-effective, facile, and reliable nucleic acid assay for mass screening to control and prevent the spread of emerging pandemic diseases. This urgent need is not fully met by current diagnostic tools. In this review, we summarize the current state-of-the-art research in novel nucleic acid amplification and detection that could be applied to point-of-care (POC) diagnosis and mass screening of diseases.

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